ID   DSBI_CAMFF              Reviewed;         215 AA.
AC   A0RN51;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Putative protein-disulfide oxidoreductase DsbI;
GN   Name=dsbI; OrderedLocusNames=CFF8240_0434;
OS   Campylobacter fetus subsp. fetus (strain 82-40).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=82-40;
RA   Fouts D.E., Nelson K.E.;
RT   "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for disulfide bond formation in some proteins. Part
CC       of a redox system composed of DsbI and DsbL that mediates formation of
CC       an essential disulfide bond in AssT (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DsbL. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DsbB family. DsbI subfamily. {ECO:0000305}.
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DR   EMBL; CP000487; ABK82964.1; -; Genomic_DNA.
DR   RefSeq; WP_002848655.1; NC_008599.1.
DR   AlphaFoldDB; A0RN51; -.
DR   STRING; 360106.CFF8240_0434; -.
DR   EnsemblBacteria; ABK82964; ABK82964; CFF8240_0434.
DR   GeneID; 61064278; -.
DR   KEGG; cff:CFF8240_0434; -.
DR   eggNOG; COG1495; Bacteria.
DR   HOGENOM; CLU_090583_1_0_7; -.
DR   OMA; CGYDNPI; -.
DR   OrthoDB; 1859420at2; -.
DR   Proteomes; UP000000760; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.20.1550.10; -; 1.
DR   InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR   InterPro; IPR023380; DsbB-like_sf.
DR   Pfam; PF02600; DsbB; 1.
DR   SUPFAM; SSF158442; SSF158442; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Disulfide bond; Electron transport;
KW   Membrane; Oxidoreductase; Redox-active center; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..215
FT                   /note="Putative protein-disulfide oxidoreductase DsbI"
FT                   /id="PRO_0000295640"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DISULFID        52..55
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..147
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  24299 MW;  18AC4230E57E403F CRC64;
     MEFFKDLKSD PIGKVASLQD ERAIWIIMVV AMSGLVIVAH SLFQNYVYMA PCEQCVYIRF
     SMLVMALGGV IAAINPKNII LKIIGYVLGF YGAIIGMMYC IKLNSIHHAV HSEDPFGVQG
     CSAEPSFPFG LPLDMWAPDW FKPTGDCGYD NPIVPDDVSL SWLQQWFVDF YSEGWYLIPS
     LKFMNMAQAC FIAYAVAFIL LFAMFICWIL KLKRA